ID A0A3Q4NBJ4_NEOBR Unreviewed; 337 AA.
AC A0A3Q4NBJ4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Methionine adenosyltransferase 2 subunit beta {ECO:0000256|ARBA:ARBA00021596, ECO:0000256|RuleBase:RU364081};
DE AltName: Full=Methionine adenosyltransferase II beta {ECO:0000256|ARBA:ARBA00029977, ECO:0000256|RuleBase:RU364081};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000031779.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000031779.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Regulatory subunit of S-adenosylmethionine synthetase 2, an
CC enzyme that catalyzes the formation of S-adenosylmethionine from
CC methionine and ATP. Regulates MAT2A catalytic activity by changing its
CC kinetic properties, increasing its affinity for L-methionine.
CC {ECO:0000256|RuleBase:RU364081}.
CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis;
CC S-adenosyl-L-methionine from L-methionine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005224, ECO:0000256|RuleBase:RU364081}.
CC -!- SUBUNIT: Heterotrimer; composed of a catalytic MAT2A homodimer that
CC binds one regulatory MAT2B chain. Heterohexamer; composed of a central,
CC catalytic MAT2A homotetramer flanked on either side by a regulatory
CC MAT2B chain. NADP binding increases the affinity for MAT2A.
CC {ECO:0000256|RuleBase:RU364081}.
CC -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose reductase family.
CC MAT2B subfamily. {ECO:0000256|ARBA:ARBA00008656,
CC ECO:0000256|RuleBase:RU364081}.
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DR AlphaFoldDB; A0A3Q4NBJ4; -.
DR Ensembl; ENSNBRT00000032582.1; ENSNBRP00000031779.1; ENSNBRG00000024106.1.
DR GeneTree; ENSGT00390000006721; -.
DR OMA; RMPLMFG; -.
DR UniPathway; UPA00315; UER00080.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000024106; Expressed in brain and 8 other cell types or tissues.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05254; dTDP_HR_like_SDR_e; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR005913; dTDP_dehydrorham_reduct.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029903; RmlD-like-bd.
DR PANTHER; PTHR10491; DTDP-4-DEHYDRORHAMNOSE REDUCTASE; 1.
DR PANTHER; PTHR10491:SF4; METHIONINE ADENOSYLTRANSFERASE 2 SUBUNIT BETA; 1.
DR Pfam; PF04321; RmlD_sub_bind; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563,
KW ECO:0000256|RuleBase:RU364081};
KW Reference proteome {ECO:0000313|Proteomes:UP000261580}.
FT DOMAIN 19..280
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
FT REGION 317..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 337 AA; 37318 MW; 096C62B3B0CBC47F CRC64;
LPEFKYYLNT EELLVGAPRV LVTGATGLLG RAVCREFHSA GWTVTGTGYR RARLRLLRCD
LTDEDAVRGL LHEYKPDVIV HCAAERRPDV MERHTEAAVN LNVHATSTLA KEAATCGALF
LYISTDYVFD GRNPPYGEDD SPNPLNVYGR SKLEGEREAL RHCPGAVVLR VPVLFGEVES
VTESVVTSLY LKVQEASEES CTLDHVLQRF PTDARDVAAV CRKLSERARQ DPSIKGVFHF
SGKEQMTKYE MAVAIAQAFN LPSGHLIPVS EQPAGGALRR SEVKDIPHAV SCSGYLCPPS
HTPEAQPVYT HEEESLTHTH THTHTHTGEP HLCRSDW
//
